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Antibodies to treat cancerRelated Patent Categories: Drug, Bio-affecting And Body Treating Compositions, Immunoglobulin, Antiserum, Antibody, Or Antibody Fragment, Except Conjugate Or Complex Of The Same With Nonimmunoglobulin Material, Monoclonal Antibody Or Fragment Thereof (i.e., Produced By Any Cloning Technology), Binds Eukaryotic Cell Or Component Thereof Or Substance Produced By Said Eukaryotic Cell, Cancer CellAntibodies to treat cancer description/claimsThe Patent Description & Claims data below is from USPTO Patent Application 20060275307, Antibodies to treat cancer. Brief Patent Description - Full Patent Description - Patent Application Claims
REFERENCES TO RELATED APPLICATIONS [0001] This application claims priority from the following U.S. Provisional Patent Applications: Ser. No. 60/339,736, filed on Dec. 11, 2001, Ser. No. 60/388,956, filed Jun. 14, 2002, Ser. No. 60/399,103, filed Jul. 26, 2002, and Ser. No. 60/400,958, filed Aug. 01, 2002. The contents of these provisional applications are incorporated herein by reference in their entireties. FIELD OF THE INVENTION [0002] The present invention relates to antibodies that can be used in the treatment of cancer, including myeloma, melanoma, and small cell lung cancer. It also relates to methods for the use of such antibodies that specifically bind to tumor cells, in which they can inhibit cellular proliferation, and induce apotosis. BACKGROUND OF THE INVENTION [0003] Gangliosides are glycosphingolipids that are present in high numbers on cells of neural crest origin as well as on a wide variety of tumor cells of neuroectodermal origin. Portoukalian et al;, Eur. J. Biochem.94:19-23 (1979); Yates et al., J. Lipid Res. 20:428-436 (1979). More specifically, expression of the gangliosides GD2, GD3, and GM2 has been reported in neuroblastoma, lung small cell carcinoma, and melanoma, each of which are highly malignant neuroectodermal tumors. J. Exp. Med., 155:1133 (1982); J. Biol. Chem. 257:12752 (1982); CancerRes. 47:225 (1987); Cancer Res. 47:1098 (1987); Cancer Res. 45:2642 (1985); Proc. Natl. Acad. Sci. U.S.A. 80:5392 (1983). [0004] The chemical structure of gangliosides includes a hydrophilic carbohydrate portion (one or more sialic acids linked to an oligosaccharide) attached to a hydrophobic lipid moiety composed of a long-chain base (sphingosine) and a fatty acid (ceramide). (G is an abbreviation for ganglioside and M, D, and T are abbreviations for mono, di, and tri, respectively; for further discussion of ganglioside nomenclature, see, Lehninger, Biochemistry, pp. 294-296 (Worth Publishers, 1981) and Wiegandt, in Glycolipids: New Comprehensive Biochemistry (Neuberger et al., ed., Elsevier, 1985), pp. 199-260; see, also, FIG. 1 for a schematic of ganglioside biosynthesis). [0005] Gangliosides are believed to be involved in cell recognition, immunosuppression, adhesion and signal transduction. The ceramide portion anchors the ganglioside into the cell membrane and may, thereby, modulate intracellular signal transduction as a second messenger. The ganglioside designated GM2 is one of a group of sialic acid residue-containing glycolipids and is uniquely characterized by its presence in only trace amounts in normal cells and its upregulation in a variety of cancer cells such as, for example, lung small cell carcinoma, melanoma, and neuroblastoma. [0006] Because they are immunogenic, gangliosides have received much attention as possible vaccine targets. For example, vaccination with a GM2 ganglioside, has been shown to stimulate high levels of anti-GM2 antibodies in melanoma patients. GM2 vaccines comprising either bacilli Calmette-Gueriii (BCG) or, more recently, keyhole limpet hemagglutinin (KLH) as adjuvant have been tested in human clinical trials. Livingston et al., Proc. Natl. Acad. Sci U.S.A. 84:2911-2915 (1987); Livingston, In "Immunity to Cancer II." Eds MS Mitchell, Pub Alan L. Liss, Inc., NY; Irie et al. U.S. Patent No. 4,557,931; Kirkwood et al. J. Clin. Oncol. 19(5):1430-1436 (2001); Chapman et al. Clin. Cancer Res. 6(3):874-879 (2000). [0007] In an effort to develop a therapeutic agent against GM2-positive cells, a number of investigators have reported the production of anti-GM2 antibodies. For example, Yamaguchi et al., described the isolation of lymphocytes from a GM2-vaccinated patient and the transformation of those lymphocytes with Epstein-Barr virus to produce an antibody (designated 3-207) simultaneously reactive for both GM2 and GD2. Proc. Natl. Acad. Sci. USA 87:3333-3337 (1990). Similarly, Irie et al., disclosed a human monoclonal anti-GM2 antibody for melanoma treatment. Lancet 1:786-787 (1989); see, also, Tai et al., Proc. Nat. Acad. Sci. U.S.A. 80:5392-5396 (1983) (disclosing a human anti-GM2 monoclonal antibody designated L55) and Yamasaki et al. U.S. Pat. No. 4,965,498 (disclosing a monoclonal antibody specific to a sugar chain containing an N-glycolylneuramine acid and having the ability to bind to at least N-glycolyl GM2 ganglioside). Furthermore, Ritter et al., disclosed antibodies produced following immunization with a lipopolysaccharide antigen of Campylobacter jejuni that reportedly binds to monosialogangliosides, including both GM2 and GM1. Int. J. Cancer 66(2):184-190 (1996). [0008] Nakamura et al. have described two murine anti-GM2 monoclonal IgM antibodies, KM696 and KM697, as well as corresponding chimeric antibodies, KM966 and KM967, constructed by replacing the variable domain heavy and light chain cDNAs of a human IgGI with the corresponding variable domain heavy and light chain cDNAs of KM696 and KM697, respectively. Cancer Research 54:1511-1516 (1994); U.S. Pat. Nos. 5,830,470 and 5,874,255. These investigators also reported CDR-grafted variants of the KM696/KM966 and the KM697/KM967 antibodies designated KM8966 and KM8967, respectively. U.S. Pat. Nos. 5,939,532 and 6,042,828. Indirect immunofluorescence staining of tumor cell lines with the KM966 chimeric antibody demonstrated that GM2 was expressed on pulmonary tumor cells and leukemia cells as well as neuroectodermal origin tumor cells. SUMMARY OF THE INVENTION [0009] The invention is based on the discovery that certain antibodies, e.g., monoclonal antibodies, specifically bind to monosialo-GM2 on the surface of numerous types of tumor cells, but do not bind to other gangliosides. These monoclonal antibodies can block proliferation and induce apoptosis of tumor cells to which they specifically bind. [0010] The invention features a method of inhibiting proliferation of a myeloma tumor cell expressing a ganglioside antigen (e.g., monosialo-GM2, asialo-GM2, disialo-GM2, monosialo-GM3, disialo-GD1a, disialo-GD1b, asialo-GM1, monosialo-GM1, lysosialo-GM1, trisialo-GT1b, and disialo-GD3) in which the method includes contacting the cell with an antibody (e.g., chimeric antibody, a humanized antibody, a human antibody, a primatized antibody, DMF10.167.4, DMF10.62.3, a chimeric antibody having a variable region of DMF10.167.4, a chimeric antibody having a variable region of DMF10.62.3, a humanized antibody having all complementary determinant regions of DMF 10.67.4, and a chimeric antibody with a light chain amino acid sequence of SEQ ID NO:21 (e.g., isoleucine at linear position 52 is replaced with valine), in which and a heavy chain amino acid sequence of SEQ ID NO:22 (e.g., threonine at linear position 78 of SEQ ID NO:22 is replaced with lysine), and the antibody specifically binds to the ganglioside. [0011] The invention also features a method of inhibiting the proliferation of a cancer cell (e.g., a thymic lymphoma, T-cell lymphoma, B-cell lymphoma, melanoma, osteosarcoma, acute T-cell leukemia, small cell lung cancer, and myeloma cell) in which the method includes contacting the cell with a chimeric antibody (e.g., administered in vivo to a mammal,) that includes a light chain amino acid sequence of SEQ ID NO:21 (e.g., in which isoleucine at linear position 52 is replace with valine) and a heavy chain amino acid sequence of SEQ ID NO:22 (e.g., in which threonine at linear position 78 is replaced with lysine). [0012] The invention further features a purified chimeric antibody (e.g., an antibody that is effective in inhibiting cell proliferation of a tumor cell to which the antibody specifically binds, an antibody that is effective in inducing apoptosis in a tumor cell to which the antibody specifically binds, an antibody that binds specifically to monosialo-GM2 on the surface of a tumor cell and induces apoptosis in a monolayer, a single-cell suspension of the tumor cells, or both, an antibody that includes a light chain having the amino acid sequence of SEQ ID NO:21 and a heavy chain having the amino acid sequence of SEQ ID NO:22, or an antibody that binds specifically to monosialo-GM2 on the surface of a tumor cell and induces apoptosis in a monolayer, a single-cell suspension of tumor cells, or both), or antigen-binding fragment thereof, in which the chimeric antibody includes an amino acid sequence comprising SEQ ID NO:21 (e.g., in which isoleucine at linear position 52 is replaced with valine) or SEQ ID NO:22 (e.g., in which threonine at linear position 78 is replaced with lysine). [0013] The invention includes an purified antibody light chain that includes the sequence of SEQ ID NO:21. [0014] Additionally, the invention includes an isolated nucleic acid molecule that includes a nucleotide sequence (e.g., the nucleotide sequence comprises SEQ ID NO:8) including that encodes the antibody light chain of a purified antibody light chain (e.g., in which isoleucine at linear position 52 of the light chain consisting of SEQ ID NO:21 is replaced with valine) that includes the sequence of SEQ ID NO:21. [0015] The invention further includes an isolated nucleic acid molecule that includes a nucleotide sequence that encodes the antibody light chain in which isoleucine at linear position 52 of SEQ ID NO:21 is replaced with valine. [0016] The invention also includes a purified antibody that includes the light chain of claim that includes the sequence of SEQ ID NO:21 and a heavy chain. [0017] Also featured in the invention is a purified antibody heavy chain having the amino acid sequence of SEQ ID NO:22 (e.g., wherein a threonine at linear position 78 is replaced with a lysine). [0018] The invention further features an isolated nucleic acid molecule in which the nucleic acid molecule includes a nucleic acid sequence that encodes the antibody heavy chain having the amino acid sequence of SEQ ID NO:22 (e.g., wherein a threonine at linear position 78 is replaced with a lysine). [0019] Also featured as part of the invention is an isolated nucleic acid molecule in which the nucleic acid molecule (e.g., including the nucleic acid sequence of SEQ ID NO:7) encodes the antibody heavy chain of the amino acid sequence of SEQ ID NO:22. [0020] The invention also includes a purified antibody comprising the heavy chain having he amino acid sequence of SEQ ID NO:22. Continue reading about Antibodies to treat cancer... Full patent description for Antibodies to treat cancer Brief Patent Description - Full Patent Description - Patent Application Claims Click on the above for other options relating to this Antibodies to treat cancer patent application. ###  How KEYWORD MONITOR works... a FREE service from FreshPatents1. Sign up (takes 30 seconds). 2. Fill in the keywords to be monitored. 3. Each week you receive an email with patent applications related to your keywords. Start now! - Receive info on patent apps like Antibodies to treat cancer or other areas of interest. ### Previous Patent Application: Use of protein tyrosine phosphatase inhibitors for prevention and/or treatment of cancer Next Patent Application: Cell death-inducing agent Industry Class: Drug, bio-affecting and body treating compositions ### FreshPatents.com Support Thank you for viewing the Antibodies to treat cancer patent info. 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